G3BP1
G3BP1 (G3BP stress granule assembly factor 1, also known as G3BP or HDH-VIII) is an RNA-binding protein and ATP-dependent helicase that is essential for stress granule formation. It also contributes to innate immune sensing of foreign nucleic acids. Browse Assay Genie's current range of G3BP1 research reagents below, or read on for the biology behind the target.
G3BP1 plays an essential role in the assembly of stress granules, the membraneless compartments that store mRNAs and proteins, including stalled translation pre-initiation complexes, in response to stress. It promotes their formation by undergoing liquid-liquid phase separation (LLPS) on binding unfolded RNA, acting as a molecular switch that triggers RNA-dependent LLPS when intracellular free RNA concentrations rise.
The G3BP1 protein is also an ATP- and magnesium-dependent helicase. It unwinds DNA/DNA, RNA/DNA and RNA/RNA substrates with comparable efficiency, moving unidirectionally in the 5' to 3' direction along bound single-stranded DNA. It prefers partial duplexes with a hanging 3' tail, or tails at both ends. In vitro, it may also act as a phosphorylation-dependent, sequence-specific endoribonuclease that cleaves exclusively between cytosine and adenine, and cleaves MYC mRNA preferentially in the 3'-UTR. UniProt reports the protein in the cytosol, perikaryon, stress granules and nucleus.
In innate immunity, G3BP1 promotes the activity of CGAS and RIGI. It aids DNA binding and activation of cGAS in the DNA-triggered cGAS/STING pathway and triggers cGAS condensation. It also enhances RIGI-induced type I interferon production, probably by helping RIGI sense pathogenic RNA. NCBI Gene describes it as a member of the heterogeneous nuclear RNA-binding proteins and an element of the Ras signal transduction pathway, binding the Ras-GTPase-activating protein through its SH3 domain. This explains the earlier name GTPase activating protein (SH3 domain) binding protein 1. The G3BP1 gene has several described alternatively spliced transcript variants, and HGNC places it among RNA binding motif containing proteins and endoribonucleases. The mouse ortholog is G3bp1.
G3BP1 is essential for stress granule formation, making it a central protein for studying how cells store mRNAs and stalled translation complexes under stress.
G3BP1 undergoes RNA-dependent liquid-liquid phase separation, acting as a molecular switch that responds to rising free RNA concentrations.
G3BP1 promotes CGAS and RIGI activity, supporting studies of the cGAS/STING pathway and RIGI-induced type I interferon production.
G3BP1 unwinds DNA and RNA duplexes in an ATP-dependent manner and may cleave RNA such as MYC mRNA in vitro.
G3BP1 is essential for stress granule formation, using RNA-triggered liquid-liquid phase separation to assemble these compartments. It is also an ATP-dependent helicase and promotes CGAS and RIGI activity in innate immunity, including enhancing RIGI-induced type I interferon production.
G3BP1 is also called G3BP and HDH-VIII. UniProt names it Ras GTPase-activating protein-binding protein 1, and its earlier HGNC name was GTPase activating protein (SH3 domain) binding protein 1. NCBI Gene notes several alternatively spliced transcript variants.
The mouse ortholog is G3bp1, so rodent models can be used to study its function. The human protein's role in stress granules and innate immunity is described in UniProt; check the datasheet of any product for its validated reactivity.
Stress granule, RNA-binding, helicase and innate immune sensing targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q13283; product specifications from Assay Genie datasheets.